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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

lysin     2,6-diaminohexanoic acid

Synonyms: DL-Lysine, H-DL-Lys-OH, PubChem12390, Lysine, DL-, AGN-PC-007WTP, ...
 
 
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Disease relevance of lysine

 

Psychiatry related information on lysine

  • The lysine mutation was not found in one Moroccan Jew from Israel with Creutzfeldt-Jakob disease [6].
  • Modification of lysine is favored by reaction at pH 7 or for short reaction times at pH 9 [7].
  • Differences in pain threshold between the two sides were significantly reduced and the EMG pattern became normal following treatment with injections of local anaesthetic into tender periarticular areas and systemic administration of lysine acetylsalicylate [8].
  • The presence of lysine leads to more aggressive viral replication, overwhelming the host's defense mechanisms and resulting in high mortality rates in mice [9].
  • By assaying the calcium- and phospholipid-dependent phosphorylation of a lysine-rich histone after detergent extraction, we have determined the total protein kinase C activity in fibroblasts from patients with sporadic Alzheimer's disease, age-matched controls and young subjects [10].
 

High impact information on lysine

 

Chemical compound and disease context of lysine

 

Biological context of lysine

 

Anatomical context of lysine

  • SUMO-conjugating enzyme is seen to be resident in plasma membrane, to assemble with K2P1, and to modify K2P1 lysine 274 [26].
  • Aggregation of lysine-containing zeins into protein bodies in Xenopus oocytes [27].
  • A tRNA(Lys) with a CUU anticodon, which has a strong affinity for AAG lysine codons, is present in eukaryotic cells but absent in E. coli [28].
  • Here we found that in the mouse V(H) locus, methylation of lysine 9 on histone H3 (H3-K9), a mark of inactive chromatin, was present in non-B lineage cells but was absent in B cells [29].
  • Here, it is shown that CBP can acetylate hepatocyte nuclear factor-4 (HNF-4), a member of the nuclear hormone receptor family, at lysine residues within the nuclear localization sequence [30].
 

Associations of lysine with other chemical compounds

 

Gene context of lysine

  • Chromatin immunoprecipitation and biochemical experiments indicate that the chromodomain of Eaf3 recruits Rpd3C(S) to nucleosomes methylated by Set2 on histone H3 lysine 36, leading to deacetylation of transcribed regions [35].
  • Revealed function of Ezh2 points to a broader usage of lysine methylation in regulation of both nuclear and extra-nuclear signaling processes [36].
  • We show that CtBP is sumoylated at a single lysine [37].
  • We show that Mms2p forms a specific heteromeric complex with the UBC13-encoded E2 and is required for the Ubc13p-dependent assembly of polyubiquitin chains linked through lysine 63 [38].
  • Lysine 9 of histone H3 is methylated by SUV39H1 (ref. 2), creating a binding site for the chromo domain of HP1 (refs 3, 4) [39].
 

Analytical, diagnostic and therapeutic context of lysine

References

  1. Structure and activation of the human N-ras gene. Taparowsky, E., Shimizu, K., Goldfarb, M., Wigler, M. Cell (1983) [Pubmed]
  2. Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin. Stanley, P., Packman, L.C., Koronakis, V., Hughes, C. Science (1994) [Pubmed]
  3. Fragments of the HIV-1 Tat protein specifically bind TAR RNA. Weeks, K.M., Ampe, C., Schultz, S.C., Steitz, T.A., Crothers, D.M. Science (1990) [Pubmed]
  4. An mRNA structure in bacteria that controls gene expression by binding lysine. Sudarsan, N., Wickiser, J.K., Nakamura, S., Ebert, M.S., Breaker, R.R. Genes Dev. (2003) [Pubmed]
  5. PRDI-BF1 recruits the histone H3 methyltransferase G9a in transcriptional silencing. Gyory, I., Wu, J., Fejér, G., Seto, E., Wright, K.L. Nat. Immunol. (2004) [Pubmed]
  6. Mutation of the prion protein in Libyan Jews with Creutzfeldt-Jakob disease. Hsiao, K., Meiner, Z., Kahana, E., Cass, C., Kahana, I., Avrahami, D., Scarlato, G., Abramsky, O., Prusiner, S.B., Gabizon, R. N. Engl. J. Med. (1991) [Pubmed]
  7. Modification of arginine and lysine in proteins with 2,4-pentanedione. Gilbert, H.F., O'Leary, M.H. Biochemistry (1975) [Pubmed]
  8. Pain thresholds and electromyographic features of periarticular muscles in patients with osteoarthritis of the knee. Brucini, M., Duranti, R., Galletti, R., Pantaleo, T., Zucchi, P.L. Pain (1981) [Pubmed]
  9. PB2 amino acid at position 627 affects replicative efficiency, but not cell tropism, of Hong Kong H5N1 influenza A viruses in mice. Shinya, K., Hamm, S., Hatta, M., Ito, H., Ito, T., Kawaoka, Y. Virology (2004) [Pubmed]
  10. Reduced protein kinase C activity in sporadic Alzheimer's disease fibroblasts. Bruel, A., Cherqui, G., Columelli, S., Margelin, D., Roudier, M., Sinet, P.M., Prieur, M., Pérignon, J.L., Delabar, J. Neurosci. Lett. (1991) [Pubmed]
  11. Discoveries of vitamin B12 and selenium enzymes. Stadtman, T.C. Annu. Rev. Biochem. (2002) [Pubmed]
  12. Histone acetyltransferases. Roth, S.Y., Denu, J.M., Allis, C.D. Annu. Rev. Biochem. (2001) [Pubmed]
  13. Carnitine--metabolism and functions. Bremer, J. Physiol. Rev. (1983) [Pubmed]
  14. Reversal of Histone Lysine Trimethylation by the JMJD2 Family of Histone Demethylases. Whetstine, J.R., Nottke, A., Lan, F., Huarte, M., Smolikov, S., Chen, Z., Spooner, E., Li, E., Zhang, G., Colaiacovo, M., Shi, Y. Cell (2006) [Pubmed]
  15. Proline isomerization of histone h3 regulates lysine methylation and gene expression. Nelson, C.J., Santos-Rosa, H., Kouzarides, T. Cell (2006) [Pubmed]
  16. Aminoacylation of synthetic DNAs corresponding to Escherichia coli phenylalanine and lysine tRNAs. Khan, A.S., Roe, B.A. Science (1988) [Pubmed]
  17. Nonenzymatic glycosylation, sulfhydryl oxidation, and aggregation of lens proteins in experimental sugar cataracts. Monnier, V.M., Stevens, V.J., Cerami, A. J. Exp. Med. (1979) [Pubmed]
  18. Daily soluble aspirin and prevention of colorectal adenoma recurrence: one-year results of the APACC trial. Benamouzig, R., Deyra, J., Martin, A., Girard, B., Jullian, E., Piednoir, B., Couturier, D., Coste, T., Little, J., Chaussade, S. Gastroenterology (2003) [Pubmed]
  19. Possible dissociation of the heparin-binding and mitogenic activities of heparin-binding (acidic fibroblast) growth factor-1 from its receptor-binding activities by site-directed mutagenesis of a single lysine residue. Burgess, W.H., Shaheen, A.M., Ravera, M., Jaye, M., Donohue, P.J., Winkles, J.A. J. Cell Biol. (1990) [Pubmed]
  20. Nucleotide sequence of the asd gene of Escherichia coli: absence of a typical attenuation signal. Haziza, C., Stragier, P., Patte, J.C. EMBO J. (1982) [Pubmed]
  21. Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Czermin, B., Melfi, R., McCabe, D., Seitz, V., Imhof, A., Pirrotta, V. Cell (2002) [Pubmed]
  22. The Set1 methyltransferase opposes Ipl1 aurora kinase functions in chromosome segregation. Zhang, K., Lin, W., Latham, J.A., Riefler, G.M., Schumacher, J.M., Chan, C., Tatchell, K., Hawke, D.H., Kobayashi, R., Dent, S.Y. Cell (2005) [Pubmed]
  23. The degradation signal in a short-lived protein. Bachmair, A., Varshavsky, A. Cell (1989) [Pubmed]
  24. The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism. Parthun, M.R., Widom, J., Gottschling, D.E. Cell (1996) [Pubmed]
  25. Dot1p modulates silencing in yeast by methylation of the nucleosome core. van Leeuwen, F., Gafken, P.R., Gottschling, D.E. Cell (2002) [Pubmed]
  26. Sumoylation silences the plasma membrane leak K+ channel K2P1. Rajan, S., Plant, L.D., Rabin, M.L., Butler, M.H., Goldstein, S.A. Cell (2005) [Pubmed]
  27. Aggregation of lysine-containing zeins into protein bodies in Xenopus oocytes. Wallace, J.C., Galili, G., Kawata, E.E., Cuellar, R.E., Shotwell, M.A., Larkins, B.A. Science (1988) [Pubmed]
  28. Sequence requirements for efficient translational frameshifting in the Escherichia coli dnaX gene and the role of an unstable interaction between tRNA(Lys) and an AAG lysine codon. Tsuchihashi, Z., Brown, P.O. Genes Dev. (1992) [Pubmed]
  29. B cell-specific loss of histone 3 lysine 9 methylation in the V(H) locus depends on Pax5. Johnson, K., Pflugh, D.L., Yu, D., Hesslein, D.G., Lin, K.I., Bothwell, A.L., Thomas-Tikhonenko, A., Schatz, D.G., Calame, K. Nat. Immunol. (2004) [Pubmed]
  30. Acetylation regulates transcription factor activity at multiple levels. Soutoglou, E., Katrakili, N., Talianidis, I. Mol. Cell (2000) [Pubmed]
  31. Anticystinuric effects of glutamine and of dietary sodium restriction. Jaeger, P., Portmann, L., Saunders, A., Rosenberg, L.E., Thier, S.O. N. Engl. J. Med. (1986) [Pubmed]
  32. Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxy-terminal regulatory region. Jove, R., Kornbluth, S., Hanafusa, H. Cell (1987) [Pubmed]
  33. Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen. Lanford, R.E., Butel, J.S. Cell (1984) [Pubmed]
  34. X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions. Heiss, N.S., Knight, S.W., Vulliamy, T.J., Klauck, S.M., Wiemann, S., Mason, P.J., Poustka, A., Dokal, I. Nat. Genet. (1998) [Pubmed]
  35. Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex. Keogh, M.C., Kurdistani, S.K., Morris, S.A., Ahn, S.H., Podolny, V., Collins, S.R., Schuldiner, M., Chin, K., Punna, T., Thompson, N.J., Boone, C., Emili, A., Weissman, J.S., Hughes, T.R., Strahl, B.D., Grunstein, M., Greenblatt, J.F., Buratowski, S., Krogan, N.J. Cell (2005) [Pubmed]
  36. Polycomb group protein ezh2 controls actin polymerization and cell signaling. Su, I.H., Dobenecker, M.W., Dickinson, E., Oser, M., Basavaraj, A., Marqueron, R., Viale, A., Reinberg, D., Wülfing, C., Tarakhovsky, A. Cell (2005) [Pubmed]
  37. The polycomb protein Pc2 is a SUMO E3. Kagey, M.H., Melhuish, T.A., Wotton, D. Cell (2003) [Pubmed]
  38. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Hofmann, R.M., Pickart, C.M. Cell (1999) [Pubmed]
  39. Rb targets histone H3 methylation and HP1 to promoters. Nielsen, S.J., Schneider, R., Bauer, U.M., Bannister, A.J., Morrison, A., O'Carroll, D., Firestein, R., Cleary, M., Jenuwein, T., Herrera, R.E., Kouzarides, T. Nature (2001) [Pubmed]
  40. Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. Zhang, X., Tamaru, H., Khan, S.I., Horton, J.R., Keefe, L.J., Selker, E.U., Cheng, X. Cell (2002) [Pubmed]
  41. Topologically linked protein rings in the bacteriophage HK97 capsid. Wikoff, W.R., Liljas, L., Duda, R.L., Tsuruta, H., Hendrix, R.W., Johnson, J.E. Science (2000) [Pubmed]
  42. Regulation of abscisic acid-induced stomatal closure and anion channels by guard cell AAPK kinase. Li, J., Wang, X.Q., Watson, M.B., Assmann, S.M. Science (2000) [Pubmed]
  43. Apolipoprotein C-III(Lys58----Glu). Identification of an apolipoprotein C-III variant in a family with hyperalphalipoproteinemia. von Eckardstein, A., Holz, H., Sandkamp, M., Weng, W., Funke, H., Assmann, G. J. Clin. Invest. (1991) [Pubmed]
  44. Complex formation of platelet thrombospondin with plasminogen. Modulation of activation by tissue activator. Silverstein, R.L., Leung, L.L., Harpel, P.C., Nachman, R.L. J. Clin. Invest. (1984) [Pubmed]
 
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